ITB4_RAT
ID ITB4_RAT Reviewed; 1807 AA.
AC Q64632;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 178.
DE RecName: Full=Integrin beta-4;
DE AltName: Full=GP150;
DE AltName: CD_antigen=CD104;
DE Flags: Precursor;
GN Name=Itgb4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Sciatic nerve;
RX PubMed=9074510; DOI=10.1016/s0378-1119(96)00725-1;
RA Feltri M.L., Arona M., Scherer S.S., Wrabetz L.;
RT "Cloning and sequence of the cDNA encoding the beta 4 integrin subunit in
RT rat peripheral nerve.";
RL Gene 186:299-304(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-1071; SER-1121;
RP SER-1386; SER-1389; SER-1425 AND SER-1776, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a
CC critical structural role in the hemidesmosome of epithelial cells. Is
CC required for the regulation of keratinocyte polarity and motility.
CC ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is
CC essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this
CC binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and
CC this binding is essential for IGF2 signaling.
CC {ECO:0000250|UniProtKB:P16144}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4 associates
CC with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via
CC cytoplasmic region). Interacts (via cytoplasmic region) with DST
CC isoform 3 (via N-terminus). Interacts (via cytoplasmic domain) with DST
CC (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is found in a
CC ternary complex with NRG1 and ERBB3. ITGA6:ITGB4 is found in a ternary
CC complex with IGF1 and IGF1R. ITGA6:ITGB4 interacts with IGF2.
CC {ECO:0000250|UniProtKB:P16144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}.
CC Note=Colocalizes with DST at the leading edge of migrating
CC keratinocytes. {ECO:0000250}.
CC -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin
CC and probably also recruit BP230.
CC -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
CC proximal region, enhancing stability and cell surface expression.
CC Palmitoylation also promotes secondary association with tertaspanins
CC (By similarity). {ECO:0000250|UniProtKB:P16144}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; U60096; AAC53094.1; -; mRNA.
DR PIR; JC6319; JC6319.
DR RefSeq; NP_037312.1; NM_013180.1.
DR PDB; 6HYF; X-ray; 1.60 A; A/B/C/D=1512-1602.
DR PDBsum; 6HYF; -.
DR AlphaFoldDB; Q64632; -.
DR SMR; Q64632; -.
DR STRING; 10116.ENSRNOP00000059783; -.
DR GlyGen; Q64632; 5 sites.
DR iPTMnet; Q64632; -.
DR PhosphoSitePlus; Q64632; -.
DR PaxDb; Q64632; -.
DR PRIDE; Q64632; -.
DR GeneID; 25724; -.
DR KEGG; rno:25724; -.
DR CTD; 3691; -.
DR RGD; 2928; Itgb4.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; Q64632; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q64632; -.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-3000157; Laminin interactions.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-446107; Type I hemidesmosome assembly.
DR PRO; PR:Q64632; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; IDA:RGD.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; TAS:RGD.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0030056; C:hemidesmosome; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0008305; C:integrin complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; TAS:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR GO; GO:0031581; P:hemidesmosome assembly; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:0035878; P:nail development; ISO:RGD.
DR GO; GO:0032290; P:peripheral nervous system myelin formation; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
DR GO; GO:0043589; P:skin morphogenesis; ISO:RGD.
DR GO; GO:0061450; P:trophoblast cell migration; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR012013; Integrin_bsu-4.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 3.
DR PANTHER; PTHR10082:SF42; PTHR10082:SF42; 3.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002513; Integrin_B4; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00237; Calx_beta; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF141072; SSF141072; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Integrin; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..1807
FT /note="Integrin beta-4"
FT /id="PRO_0000016347"
FT TOPO_DOM 28..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..1807
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..73
FT /note="PSI"
FT DOMAIN 131..340
FT /note="VWFA"
FT REPEAT 457..503
FT /note="I"
FT REPEAT 504..543
FT /note="II"
FT REPEAT 544..582
FT /note="III"
FT REPEAT 583..621
FT /note="IV"
FT DOMAIN 981..1086
FT /note="Calx-beta"
FT DOMAIN 1131..1220
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1224..1323
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1514..1609
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1627..1723
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 194..199
FT /note="Involved in NRG1- and IGF1-binding"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT REGION 457..621
FT /note="Cysteine-rich tandem repeats"
FT REGION 734..751
FT /note="Palmitoylated on several cysteines"
FT /evidence="ECO:0000250"
FT REGION 1119..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16144"
FT MOD_RES 1776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..456
FT /evidence="ECO:0000250"
FT DISULFID 38..48
FT /evidence="ECO:0000250"
FT DISULFID 41..72
FT /evidence="ECO:0000250"
FT DISULFID 51..61
FT /evidence="ECO:0000250"
FT DISULFID 245..288
FT /evidence="ECO:0000250"
FT DISULFID 424..673
FT /evidence="ECO:0000250"
FT DISULFID 453..458
FT /evidence="ECO:0000250"
FT DISULFID 469..480
FT /evidence="ECO:0000250"
FT DISULFID 477..513
FT /evidence="ECO:0000250"
FT DISULFID 482..491
FT /evidence="ECO:0000250"
FT DISULFID 493..504
FT /evidence="ECO:0000250"
FT DISULFID 519..524
FT /evidence="ECO:0000250"
FT DISULFID 521..552
FT /evidence="ECO:0000250"
FT DISULFID 526..537
FT /evidence="ECO:0000250"
FT DISULFID 558..563
FT /evidence="ECO:0000250"
FT DISULFID 565..574
FT /evidence="ECO:0000250"
FT DISULFID 576..583
FT /evidence="ECO:0000250"
FT DISULFID 597..602
FT /evidence="ECO:0000250"
FT DISULFID 599..650
FT /evidence="ECO:0000250"
FT DISULFID 604..616
FT /evidence="ECO:0000250"
FT DISULFID 628..637
FT /evidence="ECO:0000250"
FT DISULFID 634..708
FT /evidence="ECO:0000250"
FT DISULFID 653..682
FT /evidence="ECO:0000250"
FT STRAND 1519..1526
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1528..1531
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1541..1550
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1557..1561
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1568..1571
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1579..1588
FT /evidence="ECO:0007829|PDB:6HYF"
FT STRAND 1596..1601
FT /evidence="ECO:0007829|PDB:6HYF"
SQ SEQUENCE 1807 AA; 200589 MW; 2EF9BD4E345829A3 CRC64;
MAGLCSSPWV KLLLAVVLSA GLPGNMANRC KKAQVKSCTE CIRVDKSCAY CTDELFKERR
CNTQADVLAA GCRGESVLVM ESSLEITENI QIDTSLHRSQ VSPQGLQVRL RPGEERNFVF
KVFEPLESPV DLYILMDFSN SMSDDLDNLK QMGQNLAKIL RQLTSDYTIG FGKFVDKVSV
PQTDMRPEKL KEPWPNSDPP FSFKNVISLT ENVEEFWDKL QGERISGNLD APEGGFDAIL
QTAVCTRDIG WRADSTHLLV FSTESAFHYE ADGANVLAGI MNRNDEKCHL DATGAYTQYK
TQDYPSVPTL VRLLAKHNII PIFAVTNYSY SYYEKLHKYF PVSSLGVLQE DSSNIVELLE
EAFYRIRSNL DIRALDSPRG LRTEVTSDTL QKTETGSFHI KRGEVGTYNV HLRAVEDIDG
THVCQLAKED QRGNIHLKPS FSDGLRMDAS VICDMCACEL QKEVQSARCH YRGDFMCGHC
VCNEGWSGKT CNCSTGSLSD TQPCLREGED KPCSGHGECQ CGRCVCYGEG RYEGHFCEYD
NFQCPRTSGF LCNDRGRCSM GECVCEPGWT GRSCDCPLSN ATCIDSNGGI CNGLGFCECG
RCHCNQRSSL YTDTTCEINY SAIRLGLCED LRSCVQCQAW GTGEKKGRTC EECNFKVKMV
DELKKAEEVV EYCSFRDEDD DCTYSYTVEG DGSPGPNSTV LVHKKKDCLP APSWWLIPLL
IFLLLLLVLL LLLCWKYCAC CKACLGLLPC CNQGHMVGFK EDHYMLRENL MASDHLDTPM
LRSGNLKGRD TVRWKITNNV QRPGFATHAA SISPTELVPY GLSLRLGRLC TENLMKPGTR
ECDQLRQEVE ENLNEVYRQV NGVHKLQQTK FRQQPNAGKK QDHTIVDTVL LAPRSAKQSL
LKLTEKQVEQ GSFHELKVAP GYYTLTAEQD ARGMVEFQEG VELVDVRVPL FIRPEDDDEK
QLLVEAIDVP VGTATLGRRL VNITIIKEQA SGIVSFEQPE YSVSRGDQVA RIPVIRHILD
NGKSQVSYST QDNTAHGHRD YVPVEGELLF YPGETWKELQ VKLLELQEVD SLLRGRQVRR
FQVQLSNPKF GARLGQPNTA TVIIGEQDET DRSLINEISA SPPLPRGDLG APQNPNAKAA
GSRKIHFNWL PPPGKPMGYR VKYWVQGDSE SEAHLLDSKV PSVELTNLYP YCDYEMKVCA
YGAHGEGPYS SLVSCRTHQE VPSEPGRLAF NVVSSTVTQL SWAEPAETNG EITAYEVCYG
LVNEDNRPIG PMKKVLVDNP KNRMLLIENL RESQPYRYTV KARNGAGWGP EREAIINLAT
QPKRPMSIPI IPDIPIVDAQ GGEDYENFLM YSDDVLRSPA SSQRPSVSDD TEHLVNGRMD
FAYPGSANSL HRMTAANVAY GTHLSPHQTH RMLSTSSTLT RDYHSLTRTD HSQSGTLPRD
YSTLTSLSSQ GLPPIWEDGR SRLPLSWTLG SWSRAQMKGV PASRGSPDSI ILAGQSAAPS
WGTDSRGAMG VPDTPTRLVF SALGPTSLKV SWQEPQCDRA LLGYSVEYQL LNGGEMHRLN
IPNPGQTSVV VEDLLPNHSY VFRVRAQSQE GWGREREGVI TIESQVHPQS PLCPLPGSAF
TLSTPSAPGP LVFTALSPDS LQLSWERPRR PNGDILGYLV TCEMAQGGGP ARTFRVDGDN
PESRLTVPGL SENVPYKFKV QARTTEGFGP EREGIITIES QDGGPFPQLG SHSGLFQNPL
QSEYSTVTST HSTTTTEPFL IDGLTLGTQR LEAGGSLTRH VTQEFVSRTL TTSGSLSTHM
DQQFFQT
